STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
ThrCCOG0498 Threonine synthase. (403 aa)    
Predicted Functional Partners:
thrB
Homoserine kinase; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily.
 
 
 0.980
serC
Phosphoserine aminotransferase; Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily.
   
 0.944
LtaA
COG2008 Threonine aldolase.
   
 0.920
LtaA-2
COG2008 Threonine aldolase.
   
 0.920
ThrA
COG0460 Homoserine dehydrogenase.
  
 
 0.796
IlvA-2
COG1171 Threonine dehydratase.
 
 
0.795
IlvA-4
COG1171 Threonine dehydratase.
 
 
0.794
IlvA-3
COG1171 Threonine dehydratase.
 
 
0.790
IlvA
COG1171 Threonine dehydratase.
 
 
0.788
ilvA
Threonine dehydratase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.
 
 
0.786
Your Current Organism:
Amycolatopsis mediterranei
NCBI taxonomy Id: 713604
Other names: A. mediterranei S699, Amycolatopsis mediterranei S699, Amycolatopsis mediterranei str. S699, Amycolatopsis mediterranei strain S699
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